Research workbench
Domain motions in groel upon binding of an oligopeptide
Analyse Domain motions in groel upon binding of an oligopeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MNF
- Type
- protein
- Length
- 7,518 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A6F5
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | — | protein | 525 | — | P0A6F5 |
| O, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2 | — | protein | 12 | — | — |
Compared structures
- 1MNF · Domain motions in GroEL upon binding of an oligopeptide · the same entry in another collection · chain E against E, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0A6F5
- Elsewhere: RCSB PDB 1MNF · PDBe 1MNF · UniProt P0A6F5
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